NMR spectroscopy brings invisible protein states into focus Export

@article{citeulike:5972835, abstract = {Molecular dynamics are essential for protein function. In some cases these dynamics involve the interconversion between ground state, highly populated conformers and less populated higher energy structures ('excited states') that play critical roles in biochemical processes. Here we describe recent advances in NMR spectroscopy methods that enable studies of these otherwise invisible excited states at an atomic level and that help elucidate their important relation to function. We discuss a range of examples from molecular recognition, ligand binding, enzyme catalysis and protein folding that illustrate the role that motion plays in 'funneling' conformers along preferred pathways that facilitate their biological function.}, author = {Baldwin, Andrew J. and Kay, Lewis E.}, citeulike-article-id = {5972835}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/nchembio.238}, citeulike-linkout-1 = {http://dx.doi.org/10.1038/nchembio.238}, day = {19}, doi = {10.1038/nchembio.238}, issn = {1552-4450}, journal = {Nature Chemical Biology}, keywords = {active, baldwin09pdf, conformations, funneling, into, states}, month = {October}, number = {11}, pages = {808--814}, posted-at = {2009-10-20 02:17:18}, priority = {2}, publisher = {Nature Publishing Group}, title = {NMR spectroscopy brings invisible protein states into focus}, url = {http://dx.doi.org/10.1038/nchembio.238}, volume = {5}, year = {2009} }

TY - JOUR ID - citeulike:5972835 L3 - citeulike-article-id:5972835 N2 - Molecular dynamics are essential for protein function. In some cases these dynamics involve the interconversion between ground state, highly populated conformers and less populated higher energy structures ('excited states') that play critical roles in biochemical processes. Here we describe recent advances in NMR spectroscopy methods that enable studies of these otherwise invisible excited states at an atomic level and that help elucidate their important relation to function. We discuss a range of examples from molecular recognition, ligand binding, enzyme catalysis and protein folding that illustrate the role that motion plays in 'funneling' conformers along preferred pathways that facilitate their biological function. IS - 11 JF - Nature Chemical Biology SN - 1552-4450 EP - 814 TI - NMR spectroscopy brings invisible protein states into focus PB - Nature Publishing Group VL - 5 SP - 808 KW - active KW - baldwin09pdf KW - conformations KW - funneling KW - into KW - states AU - Baldwin, Andrew AU - Kay, Lewis PY - 2009/10/19/ UR - http://dx.doi.org/10.1038/nchembio.238 ER -